Matrix metalloproteinases (MMP) are a family of endopeptidases whose activities depend on metal ions such as ZN++ and Ca++. Collectively, MMPs are capable of degrading all the molecular components of extracellular (ECM), the barrier separating the tumor cells from normal surrounding tissues, which is disassembled as part of the metastatic process (Lochter, A. et al. (1998) Ann N Y Acad Sci. 857:180–193). MMPs have been shown to play important roles in a variety of biological as well as pathological processes, especially in tumor cell invasion and metastasis (Kleiner, D. E. and Stelter-Stevenson, W. G. (1999) Cancer Chemother Pharmacol. 43: S42–51). Overproduction of MMps by tumor cells or surrounding stromal cells has been correlated with the metastatic phenotype. In particular, U.S. Pat. No. 6,811,955, the contents of which are herein incorporated by reference in their entirety, teaches that intact and biologically active MMPs can be detected in biological samples of cancer patients and are independent predictors of disease status. The MMP activities detected in U.S. Pat. No. 6,811,955, include, for example, MP-9 (92 kDa, gelatinase B, type IV collagenase, EC3.4.24.35) and MMP-2 (72 kDa, gelatinase A, type IV collagenase, EC3.4.24.24). Both of these MMPs have been shown to be independent predictors of tissue remodeling-associated conditions, e.g., cancer. In addition to these two major gelatinase species, several MMP activities with molecular sizes of equal to, or great than, 150 kDa were observed and were referred to as high molecular weight (hMW) MMPs. Elevated MMP levels in biological fluids, including serum, plasma, and urine from animals bearing experimental tumors or from cancer patients have also been reported in several other studies (Nakajima, M., et al., (1993) (Cancer Res. 53: 5802–7; Zucker, S., et al. (1994) Ann N Y Acad Sci 732: 248–62; Baker, T., et al. (1994) Br J Cancer. 70: 506–12; Garbisa, S., et al. (1992) Cancer Res. 52: 4548–9, 1992).